Thermo Fisher Scientific
Glycosylation represents not only one of the most common post-translational modifications of proteins but is by far the most diverse (with literally thousands of different glycans possible at a given site of modification).
In this webcast, Dr. Lance Wells of the Complex Carbohydrate Research Center, University of Georgia, will cover methods for determining sites of modification for both N- and O-linked glycosylation. He will also discuss approaches for quantitatively determining occupancy and with N-linked glycosylation expand to include N-linked type (high Mannose versus hybrid/complex). While most of the procedures for site-mapping involve the release of the glycan from the underlying polypeptide backbone, the ultimate goal is to perform direct glycopeptide analyses. Thus, in the second half of the presentation, he will focus on direct glycopeptide approaches on the Thermo Scientific - Orbitrap Fusion Lumos mass spectrometer that allow one to observe the microheterogeneity at specific sites on proteins. Methods to be covered include combinations of pseudo-neutral loss and/or oxonium ion triggered MSn events, Step-HCD, and EThcD. Software solutions are also discussed including Byonic and pGlyco 2.1.
In this webcast, you will learn the:
Dr. Lance Wells, Professor of Biochemistry & Molecular Biology Complex Carbohydrate Research Center, University of Georgia
Dr. Wells is the co-director of the ThermoFisher appointed Center of Excellence in Glycoproteomics. He received the MCP lectureship award in 2016, and has published over 125 manuscripts. He has pioneered several approaches including BEMAD, IDAWG, pseudo-NL triggered MSn, and HCD-triggered ETD for the analyses of glycans and glycoproteins.
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